QUA1_CAEEL
ID QUA1_CAEEL Reviewed; 1169 AA.
AC G5EC21;
DT 08-JUN-2016, integrated into UniProtKB/Swiss-Prot.
DT 14-DEC-2011, sequence version 1.
DT 03-AUG-2022, entry version 66.
DE RecName: Full=Protein qua-1 {ECO:0000305};
DE Flags: Precursor;
GN Name=qua-1 {ECO:0000312|WormBase:T05C12.10};
GN ORFNames=T05C12.10 {ECO:0000312|WormBase:T05C12.10};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239 {ECO:0000312|Proteomes:UP000001940};
RN [1] {ECO:0000312|Proteomes:UP000001940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000312|Proteomes:UP000001940};
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [2] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL
RP STAGE.
RX PubMed=16502424; DOI=10.1002/dvdy.20721;
RA Hao L., Mukherjee K., Liegeois S., Baillie D., Labouesse M., Buerglin T.R.;
RT "The hedgehog-related gene qua-1 is required for molting in Caenorhabditis
RT elegans.";
RL Dev. Dyn. 235:1469-1481(2006).
CC -!- FUNCTION: Required for cuticle shedding and normal alae morphology and
CC localization, and subsequently larval development.
CC {ECO:0000269|PubMed:16502424}.
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle
CC {ECO:0000269|PubMed:16502424}. Secreted {ECO:0000269|PubMed:16502424}.
CC Secreted, extracellular space, extracellular matrix
CC {ECO:0000305|PubMed:16502424}. Note=Secreted by the underlying
CC hypodermis. {ECO:0000305|PubMed:16502424}.
CC -!- TISSUE SPECIFICITY: Transiently expressed in head cells.
CC {ECO:0000269|PubMed:16502424}.
CC -!- DEVELOPMENTAL STAGE: Mainly expressed in all hypodermal cells (hyp1 to
CC hyp11) from the tip of the head to the tip of the tail from late
CC embryogenesis to adulthood, and expressed in the excretory duct and
CC pore cells from the 3-fold stage of embryogenesis to adulthood.
CC Expressed in intestinal and rectal cells, sensilla support cells, and
CC transiently in the P lineage during the L1 stage of larval development.
CC Temporal expression during the molt phases from larval development
CC stage L2 to L4 with high expression prior to and during the L2 and L3
CC molt, but low expression between the molting phases, and low expression
CC after the L4 molt. {ECO:0000269|PubMed:16502424}.
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DR EMBL; BX284602; CAA91313.2; -; Genomic_DNA.
DR PIR; T23754; T23754.
DR RefSeq; NP_495725.2; NM_063324.3.
DR AlphaFoldDB; G5EC21; -.
DR SMR; G5EC21; -.
DR STRING; 6239.T05C12.10; -.
DR MEROPS; C46.A05; -.
DR EPD; G5EC21; -.
DR PaxDb; G5EC21; -.
DR PeptideAtlas; G5EC21; -.
DR EnsemblMetazoa; T05C12.10.1; T05C12.10.1; WBGene00004264.
DR GeneID; 174319; -.
DR KEGG; cel:CELE_T05C12.10; -.
DR CTD; 174319; -.
DR WormBase; T05C12.10; CE34989; WBGene00004264; qua-1.
DR eggNOG; KOG3638; Eukaryota.
DR HOGENOM; CLU_267484_0_0_1; -.
DR InParanoid; G5EC21; -.
DR OMA; SIFAGHN; -.
DR OrthoDB; 792800at2759; -.
DR PRO; PR:G5EC21; -.
DR Proteomes; UP000001940; Chromosome II.
DR Bgee; WBGene00004264; Expressed in larva and 4 other tissues.
DR GO; GO:0060102; C:collagen and cuticulin-based cuticle extracellular matrix; IDA:WormBase.
DR GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-KW.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0007267; P:cell-cell signaling; IEA:InterPro.
DR GO; GO:0016539; P:intein-mediated protein splicing; IEA:InterPro.
DR GO; GO:0018996; P:molting cycle, collagen and cuticulin-based cuticle; IMP:WormBase.
DR GO; GO:0002119; P:nematode larval development; IMP:WormBase.
DR GO; GO:0090597; P:nematode male tail mating organ morphogenesis; IMP:WormBase.
DR GO; GO:0016540; P:protein autoprocessing; IEA:InterPro.
DR InterPro; IPR001657; Hedgehog.
DR InterPro; IPR001767; Hedgehog_Hint.
DR InterPro; IPR003586; Hint_dom_C.
DR InterPro; IPR003587; Hint_dom_N.
DR InterPro; IPR036844; Hint_dom_sf.
DR InterPro; IPR006141; Intein_N.
DR Pfam; PF01079; Hint; 1.
DR PRINTS; PR00632; SONICHHOG.
DR SMART; SM00305; HintC; 1.
DR SMART; SM00306; HintN; 1.
DR SUPFAM; SSF51294; SSF51294; 1.
DR PROSITE; PS50817; INTEIN_N_TER; 1.
PE 2: Evidence at transcript level;
KW Cytoplasmic vesicle; Developmental protein; Extracellular matrix;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..1169
FT /note="Protein qua-1"
FT /evidence="ECO:0000305"
FT /id="PRO_5003475859"
FT REGION 261..338
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 368..933
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 267..307
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 368..387
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 408..427
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 507..523
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 561..589
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 612..628
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 757..775
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 830..868
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 880..933
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1169 AA; 116870 MW; 1DAF17FD2EB0BE47 CRC64;
MRRLSAILPI LLLSNFWPTV ESLNYKCHND QILVVQSFGN DTIRMHCQRL DLCGYQKLKC
DYDELQPQCG GKLNFVSHVN QKGSTAPVEH TCCNLFNPRS HHSIPTHIGN DCFIYELPDG
SSNGKKVDPA PADDAPYAVL KNPAEIPEQF DGVTGYRLRL FLLKNKSPPT LLVKGIERRL
DGYRVTICRP RCTSYDKVVN DNEGAEDGEW KAISWSSWSS SSWSTWARHA FNKAAAEGGE
AAERIRTRMP IGEKTVAGAA GATGAAGSDK SNINIHVESN GNNNNSFEGG RSSSEKSDGQ
LNREISGSSE AGAGGKGGAG ADGAAGSGAG AGAGAGTNGN INITVHTDGK SGGNAVAVAN
ANVTVNGAGG VSTTGTGAQT GNESGLGGSA GTDKAGGKKG GHGDSGDSGN NKNKDNGKGK
GKGKNDEEDE EDNGDEDGNG KGGNGGNPKG EWDDGDGDED DDGTDGGSKE SGNNGKGKGK
GSGDGDGNRN GNGDGNGRPK GDGNIKINIH SPDDNDLLEK DENGPNGKGG AGNGNGDGDK
DNNGKGNGTG DGDGDGNGNG NGLTGDGNGT GDGDNNESGN GNGDGSDKNS GAGAGTKPEN
REGGDGNGNG TGDGNGDGND NGNGSKGLGT GSGDGKGEGN KSGTPGKSDG KEDGAGSNGS
GNGKEGDGNK SGGSGKGGAG NGKSGDGSGD GKNNGNGGTG DGKDKNGKGS GSGDNDKSGT
RAAGKGNAEG NGKGNGNDGK GSGSGDGSGA GGKGDKSDSE SGNEADGKDG KKNEGAGGEA
AAGSGGANKG GSDGDDDDVD VTDVEVGTKP LTGTKLEELL AKLPNETADG NATGDGNEFG
TVQTGAKHNA ESSASGIPLV QARSNTVNGG APVPPAPGSG ATGSGTSGSG TSESVTNGSG
ATESGSTGSG TTGTGTSGTG SSGTGASAAR TSSIAGDAPQ AAVLADTPGA AGAAGGGRSN
CFSADSLVTT VTGQKRMDEL QIGDYVLVPS SGNVLKYEKV EMFYHREPKT RTNFVVLYTK
SGRKLSLTGR HLLPVAECSQ VEQYTMNPDG IDVAMRESKY AEKARKGECV LSIDESGEVI
ADEIVRVGRM TNVGIYSPMT VEGSLIVDGV LSSCFSHLES HSAHKLIFDF IYYVYNAFGL
LNTNHVDLQP IPTFVSFAQY LSKTVLPFS